PMID: 6268171Jul 24, 1981

Tonin, an esteroprotease from rat submaxillary glands

Biochimica Et Biophysica Acta
G Thibault, J Genest


Tonin is an enzyme found in the rat submaxillary glands which liberates angiotensin II from angiotensinogen, the Skeggs tetradecapeptide renin substrate, and angiotensin I. Tonin hydrolyzes benzoyl-arginine ethyl ester, benzoyl-arginine methyl ester, tosyl-arginine methyl ester, benzoyl-arginine p-nitroanilide and other small synthetic substrates at an optimum ph of 9.0. Tonin shows, however, a great specificity with respect to angiotensin I. Tonin is inhibited by diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride at high concentrations (greater than 10(-2) M) and by soybean trypsin inhibitor and aprotinin. Tonin is thus an esteroprotease of the class of the serine protease with trypsin- and chymotrypsin-like activity. Tonin belongs to the same family of enzyme as glandular kallikrein and the gamma subunit of the nerve growth factor.


Jan 1, 1981·Hypertension·M IkedaJ Genest


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May 1, 1993·The International Journal of Biochemistry·B L SlomianyA Slomiany
Jul 1, 1996·General Pharmacology·B L SlomianyA Slomiany
Oct 1, 1992·Experimental Eye Research·T OkamuraN Toda
Nov 1, 1982·Analytical Biochemistry·E S Cheng, B J Morris
Oct 29, 1982·Biochemical and Biophysical Research Communications·J L PesqueroA C Paiva
Jan 1, 1986·Archives of Oral Biology·K IkenoI Ishiguro
Mar 1, 1984·Hypertension·M Ikeda, K Arakawa
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Feb 1, 1988·European Journal of Biochemistry·N GutmanF Gauthier
May 1, 1996·Preparative Biochemistry & Biotechnology·G S Bedi

Related Concepts

Angiotensin I
Angiotensin II, Val(5)-
Angiotensin-Converting Enzyme Inhibitors
Renin Substrate Tetradecapeptide
Peptidyl-Dipeptidase A
Submandibular Gland
Substrate Specificity
Macromolecular Compounds
Rats, Laboratory

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